characterize the stability of a protein
how to characterize the stability of a protein from Trp fluorescence vs [denaturant] curves ?
A colleague of mine has taken Trp fluorescence measurements from a dimer in combination with various ligands, over a range of denaturant concentrations. The idea is that ligands which bind more tightly to the dimer will stabilize it and delay changes in fluorescence. This is what our data look like:
Trp is without a doubt the most fluorescent amino acid took after by Tyr. Its fluorescent can either increment or decrase amid folding. Trp fluorescence is regularly utilized as a mean of both determing stabiling and folding and unfolding rate, however relying upon the position of the Trp may change especially if the protein is unpredictable and fold through multiple intermediate states. Here you can check my best essay service to having a wonderful support for your composing works.